In 1894 Mörner demonstrated that there exist four different holoprotein fractions in the lens. A fraction insoluble at physiological pH was called albuminoid. Three watersoluble fractions were found: two atypical globulins (a and β crystallin) and an albumin-like fraction (γ crystallin).
The separation and elimination of the insoluble fraction from the crude extract is simple and made by centrifugation. The separation and fractionation of the watersoluble fractions is a much more complicated problem. Following Mörner, different authors have tried to establish a suitable fractionation device, mostly without any control (Krause, 1932; Woods and Burky, 1927; Burky and Woods, 1928; Bonot and Nordmann, 1946; Nordmann, 1949). On the other hand, the proteins by these methods of fractionation are often profoundly modified and even largely denaturated by the different manipulations. The aim of this work is to obtain well-defined and homogeneous protein fractions from the point of view of electrophoretic control.
FRANÇOIS J, RABAEY M, WIEME RJ. New Method for Fractionation of Lens Proteins. AMA Arch Ophthalmol. 1955;53(4):481-486. doi:10.1001/archopht.1955.00930010483004